Synthesis of low molecular weight heat shock peptides stimulated by ecdysterone in a cultured Drosophila cell line.
Treatment of Schneider's line 3 Drosophila cells with the steroid hormone ecdysterone rapidly stimulated the synthesis and accumulation of the polypeptide previously designated p7 [Berger, E. M., Ireland, R. C. & Wyss, C. (1980) Somatic Cell Genet. 6, 119-129]. In this report, p7 is identified as the 23,000-dalton heat shock polypeptide (hsp23). In addition to hsp23, the synthesis of the low molecular weight heat shock polypeptides hsp22, hsp26, and hsp27 was also stimulated by ecdysterone, although to different extents. Hybridization of a nick-translated genomic clone containing the hsp23 gene to a total RNA blot showed that ecdysterone stimulation of hsp23 synthesis was the result of an increase in the hsp23 RNA content of S3 cells. We detected no effect of the hormone on the synthesis of heat shock polypeptides hsp68, hsp70, and hsp83.
D000818:Animals; D002460:Cell Line; D004331:Drosophila melanogaster; D004441:Ecdysterone / Q000494:pharmacology*; D005786:Gene Expression Regulation / Q000187:drug effects; D006360:Heat-Shock Proteins; D006358:Hot Temperature; D007526:Isoelectric Point; D007700:Kinetics; D008970:Molecular Weight; D014176:Protein Biosynthesis; D012333:RNA, Messenger / Q000378:metabolism
D006360:Heat-Shock Proteins; D012333:RNA, Messenger; D004441:Ecdysterone